Structural Identification of Individual Helical Amyloid Filaments by Integration of Cryo-Electron Microscopy-Derived Maps in Comparative Morphometric Atomic Force Microscopy Image Analysis

This publication has 39 references indexed in Scilit:

• Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril
  Proceedings of the National Academy of Sciences, 2016
• Atomic Resolution Structure of Monomorphic Aβ₄₂ Amyloid Fibrils
  Journal of the American Chemical Society, 2016
• High-speed atomic force microscopy reveals structural dynamics of amyloid β _1–42 aggregates
  Proceedings of the National Academy of Sciences, 2016
• Peptide dimer structure in an Aβ(1–42) fibril visualized with cryo-EM
  Proceedings of the National Academy of Sciences, 2015
• Infrared nanospectroscopy characterization of oligomeric and fibrillar aggregates during amyloid formation
  Nature Communications, 2015
• Tau pathology and neurodegeneration
  The Lancet Neurology, 2013
• Amyloid fibril length distribution quantified by atomic force microscopy single-particle image analysis
  Protein Engineering, Design and Selection, 2009
• Seeded growth of β-amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure
  Proceedings of the National Academy of Sciences, 2009
• Atomic structures of amyloid cross-β spines reveal varied steric zippers
  Nature, 2007
• An algorithm for straightening images of curved filamentous structures
  Ultramicroscopy, 1986